Association of the Cytoplasmic Membrane Protein XpsN with the Outer Membrane Protein XpsD in the Type II Protein Secretion Apparatus of
            <i>Xanthomonas campestris</i>
            pv. Campestris

Lee, Hsien-Ming; Wang, Kuan-Cheng; Liu, Yiling; Yew, Hsin-Yan; Chen, Lingyun; Leu, Wei-Ming; Chen, David Chanhen; Hu, Nien-Tai

doi:10.1128/jb.182.6.1549-1557.2000

Cited by 36 publications

(43 citation statements)

References 59 publications

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“…Genes encoding GspN have been identified in the gsp gene clusters of most GSP-containing bacteria, except E. chrysanthemi, P. aeruginosa, and P. alcaligenes (25,40). Besides E. chrysanthemi, Aeromonas hydrophila (34), E. carotovora (41), and K. oxytoca (13) have been found to contain gspB genes.…”

Section: Discussionmentioning

confidence: 99%

“…Recently, it was shown that two other Gsp proteins (probably) interact with the GspD secretin, i.e., XpsN (GspN) of Xanthomonas campestris (40) and OutB (GspB) of E. chrysanthemi (9). Genes encoding GspN have been identified in the gsp gene clusters of most GSP-containing bacteria, except E. chrysanthemi, P. aeruginosa, and P. alcaligenes (25,40).…”

Section: Discussionmentioning

confidence: 99%

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Exchange of Xcp (Gsp) Secretion Machineries between Pseudomonas aeruginosa and Pseudomonas alcaligenes : Species Specificity Unrelated to Substrate Recognition

et al. 2001

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Pseudomonas aeruginosa and Pseudomonas alcaligenes are gram-negative bacteria that secrete proteins using the type II or general secretory pathway, which requires at least 12 xcp gene products (XcpA and XcpP to -Z). Despite strong conservation of this secretion pathway, gram-negative bacteria usually cannot secrete exoproteins from other species. Based on results obtained with Erwinia, it has been proposed that the XcpP and/or XcpQ homologs determine this secretion specificity (M. Linderberg, G. P. Salmond, and A. Collmer, Mol. Microbiol. 20: [175][176][177][178][179][180][181][182][183][184][185][186][187][188][189][190] 1996). In the present study, we report that XcpP and XcpQ of P. alcaligenes could not substitute for their respective P. aeruginosa counterparts. However, these complementation failures could not be correlated to species-specific recognition of exoproteins, since these bacteria could secrete exoproteins of each other. Moreover, when P. alcaligenes xcpP and xcpQ were expressed simultaneously in a P. aeruginosa xcpPQ deletion mutant, complementation was observed, albeit only on agar plates and not in liquid cultures. After growth in liquid culture the heat-stable P. alcaligenes XcpQ multimers were not detected, whereas monomers were clearly visible. Together, our results indicate that the assembly of a functional Xcp machinery requires species-specific interactions between XcpP and XcpQ and between XcpP or XcpQ and another, as yet uncharacterized component(s).Many extracellular proteins produced by gram-negative bacteria are secreted by the type II secretion pathway, also called the main terminal branch (MTB) of the general secretory pathway (GSP) (49). Pseudomonas aeruginosa secretes several enzymes and toxins via this pathway (20). These proteins are translocated in two steps across the bacterial cell envelope.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Exchange of Xcp (Gsp) Secretion Machineries between Pseudomonas aeruginosa and Pseudomonas alcaligenes : Species Specificity Unrelated to Substrate Recognition

et al. 2001

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“…Subsequently, the mutated xpsM gene was introduced into X. campestris pv. campestris genome following the procedures of Kamoun et al (17) with slight modifications as described elsewhere (19). Southern blot analysis of chromosomal DNA digested with ApaI and with HindIII in combination with EcoRI confirmed that only the mutated xpsM gene was present in the genome.…”

Section: Methodsmentioning

confidence: 99%

“…All antisera were prepared from rabbits. Antiserum against XpsN was prepared as described previously (19) and used in immunoblot reactions at 1:250. Antiserum against purified ␣-amylase was used at 1:500.…”

Section: Methodsmentioning

confidence: 99%

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Involvement of the XpsN Protein in Formation of the XpsL-XpsM Complex in Xanthomonas campestris pv. campestris Type II Secretion Apparatus

Lee

Tyan²,

Leu

et al. 2001

J Bacteriol

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The xps gene cluster is required for the second step of type II protein secretion in Xanthomonas campestris pv. campestris. Deletion of the entire gene cluster caused accumulation of secreted proteins in the periplasm. By analyzing protein abundance in the chromosomal mutant strains, we observed mutual dependence for normal steady-state levels between the XpsL and the XpsM proteins. The XpsL protein was undetectable in total lysate prepared from the xpsM mutant strain, and vice versa. Introduction of the wild-type xpsM gene carried on a plasmid into the xpsM mutant strain was sufficient for reappearance of the XpsL protein, and vice versa. Moreover, both XpsL and XpsM proteins were undetectable in the xpsN mutant strain. They were recovered either by reintroducing the wild-type xpsN gene or by introducing extra copies of wild-type xpsL or xpsM individually. Overproduction of wild-type XpsL and -M proteins simultaneously, but not separately, in the wild-type strain of X. campestris pv. campestris caused inhibition of secretion. Complementation of an xpsL or xpsM mutant strain with a plasmid-borne wild-type gene was inhibited by coexpression of XpsL and XpsM. The presence of the xpsN gene on the plasmid along with the xpsL and the xpsM genes caused more severe inhibition in both cases. Furthermore, complementation of the xpsN mutant strain was also inhibited. In both the wild-type strain and a strain with the xps gene cluster deleted (XC17433), carrying pCPP-LMN, which encodes all three proteins, each protein coprecipitated with the other two upon immunoprecipitation. Expression of pairwise combinations of the three proteins in XC17433 revealed that the XpsL-XpsM and XpsM-XpsN pairs still coprecipitated, whereas the XpsL-XpsN pair no longer coprecipitated.

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XylellaGenomics and Bacterial Pathogenicity to Plants

Dow

Daniels

2000

Yeast

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Xylella fastidiosa, a pathogen of citrus, is the first plant pathogenic bacterium for which the complete genome sequence has been published. Inspection of the sequence reveals high relatedness to many genes of other pathogens, notablyXanthomonas campestris. Based on this, we suggest thatXylellapossesses certain easily testable properties that contribute to pathogenicity. We also present some general considerations for deriving information on pathogenicity from bacterial genomics.

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Association of the Cytoplasmic Membrane Protein XpsN with the Outer Membrane Protein XpsD in the Type II Protein Secretion Apparatus of Xanthomonas campestris pv. Campestris

Cited by 36 publications

References 59 publications

Exchange of Xcp (Gsp) Secretion Machineries between Pseudomonas aeruginosa and Pseudomonas alcaligenes : Species Specificity Unrelated to Substrate Recognition

Exchange of Xcp (Gsp) Secretion Machineries between Pseudomonas aeruginosa and Pseudomonas alcaligenes : Species Specificity Unrelated to Substrate Recognition

Involvement of the XpsN Protein in Formation of the XpsL-XpsM Complex in Xanthomonas campestris pv. campestris Type II Secretion Apparatus

XylellaGenomics and Bacterial Pathogenicity to Plants

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